The stabilisation of Escherichia coli penicillin G acylase (PGA) by dextran polymers (of molecular weight 11.5, 37.7 and 71 kDa) was studied. The inactivation of both the native and dextrancontaining enzyme preparations obeyed ยฎrst-order kinetics at the temperature and pH values studied. The optimal
Factors affecting the synthesis of penicillins by the immobilized penicillin acylase from Escherichia coli
โ Scribed by K. P. Koteva; K. D. Ganchev
- Publisher
- John Wiley and Sons
- Year
- 1994
- Tongue
- English
- Weight
- 350 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0138-4988
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Several techniques for protein extraction were tested for recovering penicillin acylase from a recombinant strain of Escherichia coli. These techniques include chemical [guanidine hydrochloride, Triton X-100, ethylenediaminetetraacetic acid (EDTA), ethanol/toluene], physical (sonication, freeze-and-
## Abstract Highโlevel expression of recombinant penicillin acylase (PAC) using the strong __trc__ promoter system in __Escherichia coli__ is frequently limited by the processing and folding of PAC precursors (proPAC) in the periplasm, resulting in physiological stress and inclusion body formation